Coupling astogenic aging in the colonial tunicate Botryllus schlosseri with the stress protein mortalin

Dev Biol. 2018 Jan 1;433(1):33-46. doi: 10.1016/j.ydbio.2017.10.023. Epub 2017 Nov 8.

Abstract

Botryllus schlosseri, a colonial marine invertebrate, exhibits three generations of short-lived astogenic modules that continuously grow and die throughout the colony's entire lifespan, within week-long repeating budding cycles (blastogenesis), each consisting of four stages (A-D). At stage D, aging is followed by the complete absorption of adult modules (zooids) via a massive apoptotic process. Here we studied in Botryllus the protein mortalin (HSP70s member), a molecule largely known for its association with aging and proliferation. In-situ hybridization and qPCR assays reveal that mortalin follows the cyclic pattern of blastogenesis. Colonies at blastogenic stage D display the highest mortalin levels, and young modules exhibit elevated mortalin levels compared to old modules. Manipulations of mortalin with the specific allosteric inhibitor MKT-077 has led to a decrease in the modules' growth rate and the development of abnormal somatic/germinal morphologies (primarily in vasculature and in organs such as the endostyle, the stomach and gonads). We therefore propose that mortalin plays a significant role in the astogeny and aging of colonial modules in B. schlosseri, by direct involvement in the regulation of blastogenesis.

Keywords: Apoptosis; Blastogenesis; Botryllus schlosseri; GRP75; HSP70; HSPA9; PBP74; Senescence; Stemness; Urochordata.

MeSH terms

  • Age Factors
  • Aging / metabolism
  • Animals
  • Apoptosis / physiology
  • HSP70 Heat-Shock Proteins / metabolism*
  • HSP70 Heat-Shock Proteins / physiology
  • Heat-Shock Proteins
  • Pyridines / metabolism
  • Reproduction, Asexual
  • Thiazoles / metabolism
  • Urochordata / genetics*
  • Urochordata / metabolism*

Substances

  • HSP70 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Pyridines
  • Thiazoles
  • mortalin
  • MKT 077